Measured by its binding ability in a functional ELISA. Immobilized human LRPAP at 0.5 µg/mL can bind rmVLDLR (Catalog # 2258-VL) with an apparent KD <0.25 nM.
Source
E. coli-derived human LRPAP protein Tyr35-Leu357, with an N-terminal Met and a C-terminal 6-His tag
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
38.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 4296-LR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human LRPAP Protein, CF
A2MRAP
A2MRAPMRAP
A2RAP
alpha-2-macroglobulin receptor-associated protein 1
alpha-2-macroglobulin receptor-associated protein
alpha-2-MRAP
HBP44
lipoprotein receptor associated protein
low density lipoprotein receptor-related protein associated protein 1
Low density lipoprotein receptor-related protein-associated protein 1
low density lipoprotein-related protein-associated protein 1(alpha-2-macroglobulin receptor-associated protein 1)
LRPAP
LRPAP1
MGC138272
RAP
Background
LRPAP (LDL receptor-related protein-associated protein 1; also named RAP), is a ubiquitously expressed 39 kDa chaperone for LDL receptor family proteins (1, 2). Mature human LRPAP shares 77% amino acid sequence identity with mouse and rat LRPAP. It is organized into three domains of comparable length. Domains D2 and D3 interact with each other, while D1 is independent (3). The D1 domain contains a low affinity binding site for LRP, and the associated D2 and D3 domains bind LRP with high affinity (4). The majority of LRPAP is localized in the endoplasmic reticulum and Golgi (5). LRPAP prevents the premature interaction of LRP, LRP2/megalin, and VLDLR with their coexpressed ligands, thereby promoting proper receptor folding and export from the ER (6 - 8). Protonation of conserved histidine residues within the D3 domain induces the separation of LRPAP and LRP in the relatively acidic Golgi (9). LRPAP, which contains a C-terminal HNEL motif, can then recycle to the ER (9). A minor amount of LRPAP remains associated with LRP and can modulate receptor activity on the cell surface (5). Exogenously applied LRPAP competitively inhibits LDL receptor family binding and uptake of activated alpha 2-macroglobulin, apoB100- or apoE-enriched LDL and VLDL particles, cholesteryl esters, and complexes of PAI-1 with either tPA or uPA (10 - 14).
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Bu, G. (2001) Int. Rev. Cytol. 209:79.
Lazic, A. et al. (2003) Biochemistry 42:14913.
Lazic, A. et al. (2006) Arch. Biochem. Biophys. 450:167.
Bu, G. et al. (1994) J. Biol. Chem. 269:29874.
Willnow, T.E. et al. (1996) EMBO J. 15:2632.
Bu, G. and S. Rennke (1996) J. Biol. Chem. 271:22218.
Obermoeller, L.M. et al. (1997) J. Biol. Chem. 272:10761.
Lee, D. et al. (2006) Mol. Cell 22:423.
Williams, S.E. et al. (1992) J. Biol. Chem. 267:9035.
Medh, J.D. et al. (1995) J. Biol. Chem. 270:536.
Herz, J. et al. (1991) J. Biol. Chem. 266:21232.
Mokuno, H. et al. (1994) J. Biol. Chem. 269:13238.
Orth, K. et al. (1992) Proc. Natl. Acad. Sci. 89:7422.
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